Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-2-14
pubmed:abstractText
A phenol sulfotransferase (3-phosphoadenylylsulfate:phenol sulfotransferase, EC 2.8.2.1) has been purified from rat liver using an affinity chromatography system consisting of a p-hydroxyphenylacetic acid-agarose conjugate. The ligand was separated from the insoluble matrix using a spacer of approx. 25 A degrees. When this affinity system was used in conjunction with other chromatography procedures, e.g., DEAE-cellulose and Sephacryl S-200, a 630-fold purification of the enzyme was achieved. The enzyme had a molecular weight of 69 000 as determined by gel filtration and 70 000 as determined by SDS-polyacrylamide gel electrophoresis. The enzyme readily sulfates p-nitrophenol, 2-naphthol, 1-naphthol, and salicylamide, as well as naturally occurring catecholamines. Using p-nitrophenol as the substrate, the pH optimum was determined to be in the range of 5.5 to 6.4. The Km value determined for p-nitrophenol was 3.6 microM, and that for 3'-phosphoadenosine 5'-phosphosulfate was 2.5 microM. Adenosine 3',5'-bisphosphate was found to be a strong product inhibitor with Ki = 0.4 microM.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
708
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
272-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Phenol sulfotransferase. I. Purification of a rat liver enzyme by affinity chromatography.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't